Lipase colipase

For an example of neutron diffraction applied to a crystallographic problem, see D. Pignol, J. Hermoso, B. Kerfelec, I. Crenon, C. Chapus, and J. C. Fontecilla-Camps, The lipase/colipase complex is activated by a micelle Neutron crystallographic evidence, Chem. Phys. Lipids 93, 123-129, 1998. 

Patton, J.S. and Carey, M.C. 1981. Inhibition of human pancreatic lipase-colipase activity by mixed bile salt-phospholipid micelles. Am. J. Physiol. 241, G328-G336. 

Young, S.C. and Hui, D.Y. 1999. Pancreatic lipase/colipase-mediated triacylglycerol hydrolysis is required for cholesterol transport from lipid emulsions to intestinal cells. Biochem. J. 339,... 

It is dear that the interconnection between the activities of the different lipolytic enzymes, where the first enzyme modifies the physicochemical state of the lipid substrate in such a way that it becomes available to another enzyme, is not only of prime importance for lipid digestion, but also results in a broad synergism between gastric lipase, colipase, pancreatic lipase, phospholipase As. calcium, caiboxylester Lipase, bite salts, and substrate interraecK tes [55,62-64]. 

Q. Chen, B. Stemby, B. Akesson, and A. Nilsson. Effects of human poncreftlc lipase-colipase and carboxyl ester lipase on eicosapentamoic and aiachidontc acid ester bonds of triacylglycerols rich in fish oil fatty adds. Biochim. Bbphys. Acta 7044 111(1990). 

Isolated enzyme deficiencies, lipase, colipase, enterokinase Pancreatic insufficiency secondary to other disorders Celiac disease... 

Egloff, M.-P., Marguet, F., Buono, G., Verger, R., Cambillau, C. and van Tilbeurgh, H. (1995) The 2.46 A resolution structure of the pancreatic lipase-colipase complex inhibited by a Cu alkyl phosphonate. Biochemistry 34, 2751-2762... 

Bezzine, S., Ferrato, F., Ivanova, M.G., Lopez, V., Verger, R. and Carriere, F. (1999) Human pancreatic lipase colipase dependence and interfacial binding of lid domain mutants. Biochemistry 38, 5499-5510. 

Patton JS and Carey MC. Inhibition of Human Pancreatic Lipase-Colipase Activity by Mixed Bile Salt-Phospholipid Micelles. Am J Physiol 1981 241 G328-G336. 

Topical pancreatic lipase substrates like tributyrin and triolein emulsions are hydrolyzed by carboxylester lipase in the presence of bile salt but slowly—at a rate lower than 3% and 0.5%, respectively, of that observed with the lipase-colipase complex. On the other hand, the positional specificity is not restricted all three sn positions of triglycerides can be split by the carboxylester lipase. While long-chain phospholipids are resistant, short-chain phospholipids are readily attacked by carboxylester lipase [40]. The low substrate specificity of carboxylester lipase makes possible an essential role for this enzyme in the hydrolysis of triglycerides containing certain esterified polyunsaturated fatty acids, such as eicosapentaenoic, arachidonic, or linoleic acids [41], and which may be resistant to attack by pancreas lipase (see p. 190). 

Pancreatin is described in the different pharmacopeia as a slightly brown, amorphous powder with a faint, characteristic odor. It is slowly and incompletely soluble in water it is not recommended to filter the solution as the lipolytic enzymes and part of the proteolytic activity may be retained on the filter. Most pharmacopeia stipulate the minimum units of amylase (12,000 FIP units/g), lipase (15,000 FIP units/g), and protease (1000 FIP units/g) activity, but give no specifications on the content of the other components such as phospholipase A2, carboxylester lipase, colipase, and individual proteolytic enzymes. It... 

FIGURE 6.7 Lipase/colipase degradation of SLN with different matrix lipids CP, cetyl pahnitate D116, Dynasan 116 D118, Dynasan 118 NaCh, sodium cholate E80, Lipoid E80 407, poloxamer 407 Tween 80, polysorbate 80. The hpid concentration was 5% and the surfactant concentration 0.5%. The values for free fatty acids after 120 min of incubation are given. 

Photon Correlation Spectroscopy Diameters of Dynasan 114 Solid Lipid Nanoparticles with Different Surfactants (10% Lipid, 1% Surfactant) to Assess the Influence of Different Surfactants on the Enzymatic Degradation (Lipase/Colipase) of Solid Lipid Nanoparticles... 

The encapsulation of chitosan nanoparticles within liposomes and niosomes for its protection from low pH gastric medium was achieved by our group (Jain et al. 2006). It was hypothesized that though phospholipids or surfactants in vesicular form are thought to be unstable in the gastrointestinal environment, it has been reported that gastric lipases do not hydrolyze phospholipids or lipoidal surfactants. The digestion of these lipids takes place mainly in the small intestine by pancreatic lipase, colipase, phospholipase A2 and cholesterol esterase and by the action of bile salts. Thus, vesicular systems apparently provide protection to chitosan nanoparticles in the stomach, while in the intestine, the particles may get or remain encapsulated sequestered and taken by M-cells of the Peyer s patches due to their size as well as bioadhesive nature. 

FIG. 3 Structure of human pancreatic lipase-colipase complex in the closed conformation (E), and structure of the complex in the open conformation (E S). These two figures show the conformational changes in the lid, the 35-loop, and the cohpase during... 

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